240,627 research outputs found
On the lifts of F(2K S; S)structure satisfying F2KS FS 0; (F 6 0; K 1 1; S 1 1) on cotangent and tangent bundle
No full textThis paper consists of two main sections. In the first part, we find the integrability conditions bycalculating Nijenhuis tensors of the horizontal lifts of F(2K S; S)structure Satisfying F2KS FS 0. Later, we get the results of Tachibana operators applied to vector and covector fieldsaccording to the horizontal lifts of F(2K S; S)structure in cotangent bundle T(Mn). Finally,we have studied the purity conditions of Sasakian metric with respect to the horizontal lifts of thestructure. In the second part, all results obtained in the first section were obtained according to thecomplete and horizontal lifts of F(2K S; S)structure in tangent bundle T(Mn)
Semi cotangent demette F NF 2 cc 1 - c h yap s na göre tachibana operatörleri ve integrallenebilme artlar
No full textThe main aim of this paper is to find integrability conditions by calculating Nijenhuis Tensors N X, , Y N X N , , , cc cc cc vv vv vv h h ihofalmost complex structure F NF 2 cc 1 - c h and to show the results of Tachibana operators applied ccX and vvw according to structureF NF 2 cc 1 - c h in semi cotangent bundle t*(Mn).The main aim of this paper is to find integrability conditions by calculating Nijenhuis Tensors N X, , Y N X N , , , cc cc cc vv vv vv h h ihof almost complex structure F NF 2 cc 1 - c h and to show the results of Tachibana operators applied ccX and vvw according to structure F NF 2 cc 1 - c h in semi cotangent bundle t*(Mn )
HA-Hipk and Stat92E-MYC physically interact in the wing imaginal disc.
No full textProximity Ligation Assays (PLA) were performed on L3 wing imaginal discs by probing with antibodies against HA and MYC tags to detect HA-Hipk and Stat92E-MYC, respectively. A positive PLA signal is observed along the dpp domain in (A, B) dpp>HA-hipk1M+Stat92E-MYC and (C,D) dpp>MYR-HA-hipk+Stat92E-MYC discs, but not in (E,F) dpp>NLS-HA-hipk+Stat92E-MYC discs. Boxed regions in A, C, E represent zoomed-in regions in B, D, F. Images in C, D represent a membrane focal plane, and thus exclude the DAPI stained nuclei. Scale bars equal 10μm.</p
Variations on the Author
No full text“Variations on the Author” discusses two of Eduardo Coutinho’s recent films (Um Dia na Vida, from 2010, and Últimas Conversas, posthumously released in 2015) and their contribution to the general question of documentary authorship. The director’s filmography is characterized by a consistent yet self-effacing form of authorial self-inscription: Coutinho often features as an interviewer that rather than express opinions propels discourses; an interviewer that is good at listening. This mode of self-inscription characterizes him as an author who is not expressive but who is nonetheless markedly present on the screen. In Um Dia na Vida, however, Coutinho is completely absent form the image, while Últimas Conversas, on the contrary, includes a confessional prologue that moves the director from the margins to the center of his films. This article examines the ways in which these works stand out in the filmography of a director who offers new insights into the notion of cinematic authorship
Petites Pieces pour le Piano-Forte / composées par F. G. Ha¨yn
No full textPETITES PIECES POUR LE PIANO-FORTE / COMPOSÉES PAR F. G. HA¨YN
Petites Pieces pour le Piano-Forte / composées par F. G. Ha¨yn (1)
Titelseite (1)
Noten (2
HA-protomer movement and mutagenesis.
No full textEach H7.5 Fab was found to recognize a primary epitope on one HA1 subunit and a second smaller region on an adjacent HA1 subunit. (A) The variable domain of one H7.5 Fab is shown as a purple surface for the heavy chain and as a light purple surface for the light chain. The HA1 subunit primarily recognized by H7.5 Fab is shown as a dark green surface, with the epitope surface color in orange (surface 1). The adjacent subunit that is also contacted by the same Fab was colored in light green, with the epitope region in yellow (surface 2). (B) Top view of the H7.5 epitope on H7 HA before and after H7.5 binding. The estimated buried area surfaces on each HA1 subunit and its predicted Gibbs free energies upon H7.5 binding were analyzed. (C) Interaction between Fab H7.5 and HA primary binding surface 1. The H7.5 antibody is shown as main-chain trace, with the interacting residues that are critical to the H7 recognition shown in sticks. The HA1 subunit with surface 1 is shown in a main-chain trace. The main chain and side chain of H7 HA residues that form direct contacts with H7.5 are shown in stick representation. (D) Interaction between two adjacent protomers and a single Fab. When the H7.5 antibody (purple) is docked onto the closed HA (green) head conformation exhibited in 3M5G, there is a clash with the adjacent protomer (top panel). When the 3M5G HA head is morphed into our model, the increased spacing between the heads alleviates this clash, thereby accommodating the CDRH3 loop (bottom panel). (E) The Kd values of H7.5 or mutated H7.5 Fab binding to the HA1 subunit of H7 (A/Shanghai/2/2013) by biolayer interferometry. (F) Sequence alignment of H7 strains with H3N2 reference strain showing the H7.5 epitope (highlighted in yellow) is well conserved among H7. (G) Amino acid sequence analysis of H7.5 epitope among 13,880 influenza A HA sequences obtained from www.fludb.org showing poor conservation in the H7.5 epitope in subtypes other than H7. CDRH3, complementarity determining region heavy chain 3; Fab, fragment antigen binding; HA, hemagglutinin.</p
HA-COMTD1 does not localize to melanosomes or endolysosomes.
No full textImmortalized melan-Ink4a cells were transiently transfected to express COMTD1 fused with the HA11 epitope at the N-terminus (HA-COMTD1) (A-D) or the HA11 epitope at the C-terminus (COMTD1-HA) (E-H). Two days later, cells were fixed and analyzed by bright field (BF) and dIFM for HA and markers of either mature melanosomes (TYRP1; A, E), early stage melanosomes (PMEL; B, F), late endosomes/ lysosomes (LAMP2 C, G), or early endosomes (STX13; D, H). Individual images of labeled cells or the bright field image are shown in addition to an overlay of HA (green) with the indicated marker (red). Insets show a 7-fold magnified image of the boxed region to emphasize the lack of overlap. Main scale bar, 10 μm; inset scale bar, 2 μm. (PDF)</p
[Newspaper Clipping: Author Claims Evidence of Second JFK Assassin #1]
No full textNewspaper article titled "Author Claims Evidence of Second JFK Assassin." The article states that author Richard J. Whalen concluded "that there is circumstantial evidence to support the theory of a second assassin in the shooting of President John F. Kennedy.
HA-tagging, localization and complex formation of PkRIPR.
No full text(A) Schematic of single homologous recombination to generate C-terminally tagged parasite line, PkRIPR-HA. (B) Integration PCRs using genomic DNA from PkA1-H.1 (PK wt) parasites or PkRIPR-HA parasite clones I1 and G4. Using the primer pair PkRIPRextF1/PkRIPRutrRev, a 1595 bp fragment was amplified from wild type parasites, whereas primer pair PkRIPRextF1/HArev amplified a 1526 bp fragment only from transgenic PkRIPR-HA parasites. Positions of primer pairs are indicated in schematic (A) and size standards (kb) on the left of the gel (B). Primers used were PkRIPRextF1 (1), PkRIPRutrRev (2), HArev (3). (C) Southern blot of wildtype and transgenic parasite DNA digested with EcoRV/AvaI. Endogenous locus band, integration and episomal bands are indicated with arrows. (D) Immunoblot of purified schizont material solubilized in Laemmli sample buffer probed with anti-BiP and anti-HA (3F10) antibodies. Molecular mass standards are indicated on the left in kDa. (E) IFAs of schizonts and merozoites with micronemes not secreted (2nd row) or secreted (3rd row) were probed with anti-HA antibody (green), anti-PkAMA1 antibody, or anti-PkRhopH2 antibody (both red) and DAPI (Blue). The third panel shows an overlay of DAPI marking the nucleus with anti-HA and anti-PkAMA1; the fourth panel includes a differential interference contrast (DIC) image of the whole parasite. Scale bar = 2 μm. (F) Table of proteins interacting with PkRIPR-HA as identified by LC-MS/MS following immunoprecipitation. The three top-scoring, consistently identified proteins are listed. The number of peptides of three technical replicates of immunoprecipitates from PkRIPR-HA clone G4 or wild type parasites is displayed, as is the total peptide coverage, gene IDs and annotations (PlasmoDB release 25).</p
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